CENPF References External links Further reading Navigation menuCENPF131330222969CENPFprotein...

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Genes on human chromosome 1Human chromosome 1 gene stubs


1063108000ENSG00000117724ENSMUSG00000026605P49454proteingene






























































CENPF
Identifiers
Aliases
CENPF, CENF, PRO1779, hcp-1, CILD31, STROMS, centromere protein F
External IDs MGI: 1313302 HomoloGene: 22969 GeneCards: CENPF


















Gene location (Human)
Chromosome 1 (human)
Chr. Chromosome 1 (human)[1]

Chromosome 1 (human)
Genomic location for CENPF

Genomic location for CENPF

Band 1q41 Start 214,603,195 bp[1]
End 214,664,588 bp[1]

































Orthologs
Species Human Mouse
Entrez





Ensembl





UniProt





RefSeq (mRNA)


NM_016343




NM_001081363

RefSeq (protein)


NP_057427




n/a

Location (UCSC) Chr 1: 214.6 – 214.66 Mb Chr 1: 189.64 – 189.69 Mb

PubMed search
[3] [4]
Wikidata



View/Edit Human View/Edit Mouse

Centromere protein F is a protein that in humans is encoded by the CENPF gene.[5][6][7]


This gene encodes a protein that associates with the centromere-kinetochore complex. The protein is a component of the nuclear matrix during the G2 phase of interphase. In late G2 the protein associates with the kinetochore and maintains this association through early anaphase. It localizes to the spindle midzone and the intracellular bridge in late anaphase and telophase, respectively, and is thought to be subsequently degraded. The localization of this protein suggests that it may play a role in chromosome segregation during mitotis. It is thought to form either a homodimer or heterodimer. Autoantibodies against this protein have been found in patients with cancer or graft versus host disease.[7]



References





  1. ^ abc GRCh38: Ensembl release 89: ENSG00000117724 - Ensembl, May 2017


  2. ^ abc GRCm38: Ensembl release 89: ENSMUSG00000026605 - Ensembl, May 2017


  3. ^ "Human PubMed Reference:"..mw-parser-output cite.citation{font-style:inherit}.mw-parser-output .citation q{quotes:"""""""'""'"}.mw-parser-output .citation .cs1-lock-free a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/6/65/Lock-green.svg/9px-Lock-green.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .citation .cs1-lock-limited a,.mw-parser-output .citation .cs1-lock-registration a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/d/d6/Lock-gray-alt-2.svg/9px-Lock-gray-alt-2.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .citation .cs1-lock-subscription a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/a/aa/Lock-red-alt-2.svg/9px-Lock-red-alt-2.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration{color:#555}.mw-parser-output .cs1-subscription span,.mw-parser-output .cs1-registration span{border-bottom:1px dotted;cursor:help}.mw-parser-output .cs1-ws-icon a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/4/4c/Wikisource-logo.svg/12px-Wikisource-logo.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output code.cs1-code{color:inherit;background:inherit;border:inherit;padding:inherit}.mw-parser-output .cs1-hidden-error{display:none;font-size:100%}.mw-parser-output .cs1-visible-error{font-size:100%}.mw-parser-output .cs1-maint{display:none;color:#33aa33;margin-left:0.3em}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration,.mw-parser-output .cs1-format{font-size:95%}.mw-parser-output .cs1-kern-left,.mw-parser-output .cs1-kern-wl-left{padding-left:0.2em}.mw-parser-output .cs1-kern-right,.mw-parser-output .cs1-kern-wl-right{padding-right:0.2em}


  4. ^ "Mouse PubMed Reference:".


  5. ^ Rattner JB, Rao A, Fritzler MJ, Valencia DW, Yen TJ (Mar 1994). "CENP-F is a .ca 400 kDa kinetochore protein that exhibits a cell-cycle dependent localization". Cell Motil Cytoskeleton. 26 (3): 214–26. doi:10.1002/cm.970260305. PMID 7904902.


  6. ^ Testa JR, Zhou JY, Bell DW, Yen TJ (Mar 1995). "Chromosomal localization of the genes encoding the kinetochore proteins CENPE and CENPF to human chromosomes 4q24→q25 and 1q32→q41, respectively, by fluorescence in situ hybridization". Genomics. 23 (3): 691–3. doi:10.1006/geno.1994.1558. PMID 7851898.


  7. ^ ab "Entrez Gene: CENPF centromere protein F, 350/400ka (mitosin)".




External links


  • Human CENPF genome location and CENPF gene details page in the UCSC Genome Browser.


Further reading


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  • Ma L, Zhao X, Zhu X (2006). "Mitosin/CENP-F in mitosis, transcriptional control, and differentiation". J. Biomed. Sci. 13 (2): 205–13. doi:10.1007/s11373-005-9057-3. PMID 16456711.


  • Liao H, Winkfein RJ, Mack G, et al. (1995). "CENP-F is a protein of the nuclear matrix that assembles onto kinetochores at late G2 and is rapidly degraded after mitosis". J. Cell Biol. 130 (3): 507–18. doi:10.1083/jcb.130.3.507. PMC 2120529. PMID 7542657.


  • Li Q, Ke Y, Kapp JA, et al. (1995). "A novel cell-cycle-dependent 350-kDa nuclear protein: C-terminal domain sufficient for nuclear localization". Biochem. Biophys. Res. Commun. 212 (1): 220–8. doi:10.1006/bbrc.1995.1959. PMID 7612011.


  • Zhu X, Chang KH, He D, et al. (1995). "The C terminus of mitosin is essential for its nuclear localization, centromere/kinetochore targeting, and dimerization". J. Biol. Chem. 270 (33): 19545–50. doi:10.1074/jbc.270.33.19545. PMID 7642639.


  • Zhu X, Mancini MA, Chang KH, et al. (1995). "Characterization of a novel 350-kilodalton nuclear phosphoprotein that is specifically involved in mitotic-phase progression". Mol. Cell. Biol. 15 (9): 5017–29. doi:10.1128/MCB.15.9.5017. PMC 230749. PMID 7651420.


  • Li S, Ku CY, Farmer AA, et al. (1998). "Identification of a novel cytoplasmic protein that specifically binds to nuclear localization signal motifs". J. Biol. Chem. 273 (11): 6183–9. doi:10.1074/jbc.273.11.6183. PMID 9497340.


  • Chan GK, Schaar BT, Yen TJ (1998). "Characterization of the kinetochore binding domain of CENP-E reveals interactions with the kinetochore proteins CENP-F and hBUBR1". J. Cell Biol. 143 (1): 49–63. doi:10.1083/jcb.143.1.49. PMC 2132809. PMID 9763420.


  • Zhu X (1999). "Structural requirements and dynamics of mitosin-kinetochore interaction in M phase". Mol. Cell. Biol. 19 (2): 1016–24. doi:10.1128/MCB.19.2.1016. PMC 116032. PMID 9891037.


  • Erlanson M, Casiano CA, Tan EM, et al. (1999). "Immunohistochemical analysis of the proliferation associated nuclear antigen CENP-F in non-Hodgkin's lymphoma". Mod. Pathol. 12 (1): 69–74. PMID 9950165.


  • Goodwin RL, Pabón-Peña LM, Foster GC, Bader D (1999). "The cloning and analysis of LEK1 identifies variations in the LEK/centromere protein F/mitosin gene family". J. Biol. Chem. 274 (26): 18597–604. doi:10.1074/jbc.274.26.18597. PMID 10373470.


  • Ashar HR, James L, Gray K, et al. (2000). "Farnesyl transferase inhibitors block the farnesylation of CENP-E and CENP-F and alter the association of CENP-E with the microtubules". J. Biol. Chem. 275 (39): 30451–7. doi:10.1074/jbc.M003469200. PMID 10852915.


  • Kobayashi M, Hanai R (2001). "M phase-specific association of human topoisomerase IIIbeta with chromosomes". Biochem. Biophys. Res. Commun. 287 (1): 282–7. doi:10.1006/bbrc.2001.5580. PMID 11549288.


  • Hussein D, Taylor SS (2003). "Farnesylation of Cenp-F is required for G2/M progression and degradation after mitosis". J. Cell Sci. 115 (Pt 17): 3403–14. PMID 12154071.


  • Holstein SA, Hohl RJ (2003). "Synergistic interaction of lovastatin and paclitaxel in human cancer cells". Mol. Cancer Ther. 1 (2): 141–9. PMID 12467231.


  • Konstantinidou AE, Korkolopoulou P, Kavantzas N, et al. (2003). "Mitosin, a novel marker of cell proliferation and early recurrence in intracranial meningiomas". Histol. Histopathol. 18 (1): 67–74. PMID 12507285.


  • Yang ZY, Guo J, Li N, et al. (2004). "Mitosin/CENP-F is a conserved kinetochore protein subjected to cytoplasmic dynein-mediated poleward transport". Cell Res. 13 (4): 275–83. doi:10.1038/sj.cr.7290172. PMID 12974617.


  • Laoukili J, Kooistra MR, Brás A, et al. (2005). "FoxM1 is required for execution of the mitotic programme and chromosome stability". Nat. Cell Biol. 7 (2): 126–36. doi:10.1038/ncb1217. PMID 15654331.


  • Zhou X, Wang R, Fan L, et al. (2005). "Mitosin/CENP-F as a negative regulator of activating transcription factor-4". J. Biol. Chem. 280 (14): 13973–7. doi:10.1074/jbc.M414310200. PMID 15677469.














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